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Characterization of S-Ribosylhomocysteinase (Luxs)

Jinge Zhu

ISBN 10: 3639165152 / ISBN 13: 9783639165159
Published by VDM Verlag
New Condition: New Soft cover
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224 pages. Dimensions: 8.7in. x 5.9in. x 0.5in.S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether bond in S-ribosylhomocysteine to produce L- homocysteine and 4, 5-dihydroxy-2, 3-pentanedione, the precursor of type II bacterial quorum sensing autoinducer. This work carried out extensive mechanistic studies of the LuxS reaction. The native metal cofactor of LuxS was identified as ferrous ion, instead of previously reported zinc ion, with a potential catalytic role. Substantial evidence was provided for the internal redox reaction, which comprised two consecutive carbonyl migration steps followed by -elimination. Three LuxS activity assays were developed and greatly facilitated the mechanistic investigations of LuxS. Two classes of LuxS inhibitors were designed based on metal chelation and catalytic mechanism, respectively. They encouraged future development of LuxS inhibitors as novel antibacterial agents and helped probe the catalytic mechanism of LuxS. This item ships from multiple locations. Your book may arrive from Roseburg,OR, La Vergne,TN. Bookseller Inventory # 9783639165159

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Bibliographic Details

Title: Characterization of S-Ribosylhomocysteinase ...

Publisher: VDM Verlag

Binding: Paperback

Book Condition:New

Book Type: Paperback

About this title

Synopsis:

S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether bond in S-ribosylhomocysteine to produce L- homocysteine and 4,5-dihydroxy-2,3-pentanedione, the precursor of type II bacterial quorum sensing autoinducer. This work carried out extensive mechanistic studies of the LuxS reaction. The native metal cofactor of LuxS was identified as ferrous ion, instead of previously reported zinc ion, with a potential catalytic role. Substantial evidence was provided for the internal redox reaction, which comprised two consecutive carbonyl migration steps followed by ?-elimination. Three LuxS activity assays were developed and greatly facilitated the mechanistic investigations of LuxS. Two classes of LuxS inhibitors were designed based on metal chelation and catalytic mechanism, respectively. They encouraged future development of LuxS inhibitors as novel antibacterial agents and helped probe the catalytic mechanism of LuxS.

About the Author:

Jinge Zhu Ph.D., Biochemistry, The Ohio State University, Columbus, OH (2005); Research Associate, University of Wisconsin - Madison.

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